Search results for CDC16

Showing 13 results out of 14

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Protein (2 results from a total of 2)

Identifier: R-HSA-174156
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: CDC16: Q13042
Identifier: R-HSA-174049
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: CDC16: Q13042

Reaction (10 results from a total of 11)

Identifier: R-HSA-174119
Species: Homo sapiens
Compartment: nucleoplasm
Phosphorylation of the APC/C is believed to be required for its activation. While the identity of the essential phosphorylation sites and the kinase(s) responsible are not known with certainty, in vitro studies have shown that the Apc1 and the tetratricopeptide repeat (TPR) subunits Cdc27, Cdc16, Cdc23 and Apc7 are phosphorylated and that the Cdk1 and Plk1 kinases may play a role.
Identifier: R-HSA-174132
Species: Homo sapiens
Compartment: nucleoplasm
Phosphorylation of the APC/C is believed to be required for its activation. While the identity of the essential phosphorylation sites and the kinase(s) responsible are not known with certainty, in vitro studies have shown that the Apc1 and the tetratricopeptide repeat (TPR) subunits Cdc27, Cdc16, Cdc23 and Apc7 are phosphorylated and that the Cdk1 and Plk1 kinases may play a role.
Identifier: R-HSA-8854604
Species: Homo sapiens
Compartment: cytoplasmic vesicle membrane
RAB4A is a master regulator of receptor recycling from endocytic compartments to the plasma membrane. It is involved in transferrin receptor recycling and EGFR trafficking and signalling. TBC (Tre2/Bub2/Cdc16) domain family member 16 (TBC1D16), is a GTPase activating protein for Rab4A and enhances the intrinsic rate of GTP hydrolysis by RAB4A (Goueli et al. 2012).
Identifier: R-HSA-8854759
Species: Homo sapiens
Compartment: recycling endosome membrane
TBC (Tre2/Bub2/Cdc16) domain family, member 14 (TBC1D14) is a putative Rab GTPase activating protein (GAP) member that binds to activated Rab11 and regulates starvation-induced autophagy. TBC1D14 does not have the GAP activity and may function as Rab11 effector. TBC1D14 also colocalizes and interacts with the autophagy kinase ULK1. Overexpression of TBC1D14 causes tubulation of recycling endosomes (REs), accumulation of the ULK1 complex and Rab11 on REs, and inhibition of vesicular transport from the RE (Longatti et al. 2012).
Identifier: R-HSA-8854182
Species: Homo sapiens
Compartment: recycling endosome membrane, recycling endosome
Rab8 is a small GTPase that is specifically involved in the regulation of secretory/recycling vesicles, modulation of the actin cytoskeleton, and cell polarity. TBC (Tre2/Bub2/Cdc16) domain family member 17 (TAB1CD17), a member of the Rab GTPase-activating protein, regulates Rab8-mediated endocytic trafficking of transferrin receptor through its interaction with optineurin (OPTN) (Vaibhava et al. 2012).
Identifier: R-HSA-8854293
Species: Homo sapiens
Compartment: recycling endosome membrane, microvillus
TBC1D10A (EPI64), a RabGAP protein with a Tre-2/Bub2/Cdc16 (TBC) domain, is an effector of ARF6 and regulates ARF6-dependent membrane trafficking (Hanono et al. 2006). The TBC domain of EPI64 binds to ARF6 and stabilizes ARF6:GTP levels in a manner that is independent of its GAP activity. This interaction keeps ARF6 in an active state either by locking ARF6:GTP in an active state or may sterically hinders ARF6 from associating with its GAP, delaying the hydrolysis of bound GTP to GDP (Hokanson & Bretscher 2011).
Identifier: R-HSA-8854290
Species: Homo sapiens
Compartment: endoplasmic reticulum-Golgi intermediate compartment membrane
TBC (Tre2/Bub2/Cdc16) domain family member 20 (TBC1D20), is a member of the Rab GAP for Rab1, the Rab involved in the regulation of ER-to-Golgi transport. TBC1D20 also interacts with Hepatitis C virus (HCV) nonstructural protein NS5A and this interaction is necessary for efficient HCV infection. It has been proposed that the TBC1D20:NS5A interaction locally inactivates Rab1 at sites of nascent viral protein synthesis to promote redirection from a Golgi-bound pathway to the virus-induced membrane structures, supporting HCV RNA replication (Sklan et al. 2007).
Identifier: R-HSA-8854588
Species: Homo sapiens
Compartment: autophagosome membrane, autophagosome
TBC (Tre2/Bub2/Cdc16) domain family member 25 (TBC1D25 also referred as OATL1), a putative GTPase activating protein (GAP), is recruited to autophagosomes through an interaction with ATG8 homologues (LC3, GABARAP and GATE-16), and is involved in the fusion between autophagosomes and lysosomes through its GAP activity. OATL1 delays autophagosomal maturation by inhibiting the encounter between autophagosomes and lysosomes (Itoh et al. 2011).
Identifier: R-HSA-8854255
Species: Homo sapiens
Compartment: lysosomal membrane, cytosol
RAB7, a small GTPase of the Rab family is associated with both endosomes and lysosomes. It facilitates endosomal maturation, transport from late endosomes to lysosomes, and the positioning of endosomes and lysosomes via regulating their movement along the cytoskeleton. RAB7 is inactivated through hydrolysis of bound GTP into GDP by its intrinsic GTPase activity, which is catalysed by the activity of a GAP (GTPase activating protein).
TBC1 domain family member 2A (TBC1D2A also referred as ARMUS for variant c; PARIS1 for variant a) is a member of the TBC/RabGAP family (Tre2/Bub2/Cdc16; TBC domain) that specifically inactivates RAB7 by accelerating its GTPase activity. TBC1D2A binds specifically to activated Rac1 and its C-terminal TBC/RabGAP domain inactivates RAB7 to promote ARF6-induced E-Cadherin degradation (Frasa et al. 2010). During the regulation of autophagy, TBC1D2A is recruited to autophagosomes by interacting with LC3, a core autophagy regulator, thereby inhibiting RAB7 (Carroll et al. 2013)
Identifier: R-HSA-8854222
Species: Homo sapiens
Compartment: early endosome membrane
TBC1 domain family member 3 (TBC1D3) belongs to the TBC/RabGAPs family and contains a TBC (Tre-2/Bub2/Cdc16) domain but has no GAP activity. It regulates macropinocytosis in response to epidermal growth factor (EGF), and facilitates crosstalk between the GTPases ARF6 and RAB5 (Frittoli et al. 2008). TBC1D3 binds to the ARF6 effector protein GGA (Golgi-localized, gamma-ear-containing, ARF-binding protein), which binds to a complex consisting of the RAB5GEF, rabaptin 5-associated exchange factor for Rab5 (RABEX5), and the Rab5 effector Rabaptin-5, thereby providing an indirect interaction between TBC1D3 and RAB5. Although TBC1D3 associates with Rab5, it may operate as a Rab5 effector, and not as a Rab5 GAP (Huaiping et al. 2007, Wainszelbaum et al. 2008).

Pathway (1 results from a total of 1)

Identifier: R-HSA-8854214
Species: Homo sapiens
Rab GTPases are peripheral membrane proteins involved in membrane trafficking. Often through their indirect interactions with coat components, motors, tethering factors and SNAREs, the Rab GTPases serve as multifaceted organizers of almost all membrane trafficking processes in eukaryotic cells. To perform these diverse processes, Rab GTPases interconvert between an active GTP-bound form and an inactive, GDP-bound form. The GTP-bound activated form mediates membrane transport through specific interaction with multiple effector molecules (Zerial & McBride 2001, Stenmark 2009, Zhen & Stenmark 2015, Cherfils & Zeghouf 2013). Conversion from the GTP- to the GDP-bound form occurs through GTP hydrolysis, which is not only driven by the intrinsic GTPase activity of the Rab protein but is also catalysed by GTPase-activating proteins (GAPs). GAPs not only increase the rate of GTP hydrolysis, but they are also involved in the inactivation of RABs, making sure they are inactivated at the correct membrane. Human cells contain as many as 70 Rabs and at least 51 putative Rab GAPs (Pfeffer 2005). Only a few of these GAPs have been matched to a specific Rab substrate. The Tre-2/Bub2/Cdc16 (TBC) domain-containing RAB-specific GAPs (TBC/RABGAPs) are a key family of RAB regulators, where the TBC domain facilitates the inactivation of RABs by facilitating activation of GTPase activity of the RAB (Pan et al. 2006, Frasa et al. 2012, Stenmark 2009). Studies suggest that TBC/RABGAPs are more than just negative regulators of RABs and can integrate signalling between RABs and other small GTPases, thereby regulating numerous cellular processes like intracellular trafficking (Frasa et al. 2012).
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